Q9ULV8 · CBLC_HUMAN
- ProteinE3 ubiquitin-protein ligase CBL-C
- GeneCBLC
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids474 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Miscellaneous
Catalytic activity
Activity regulation
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase CBL-C
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9ULV8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 244 | Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 244 | No effect on interaction with EGFR and SRC as well as on SRC ubiquitination. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 264 | Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination. | ||||
Sequence: R → A | ||||||
Mutagenesis | 265 | Enhances interaction with EGFR and SRC as well as SRC ubiquitination. | ||||
Sequence: P → L | ||||||
Mutagenesis | 266 | Decreases interactions with EGFR and SRC as well as SRC ubiquitination. | ||||
Sequence: S → A | ||||||
Mutagenesis | 268 | Abolishes interaction with EGFR. Decreases interaction with and ubiquitination of SRC. | ||||
Sequence: T → A | ||||||
Mutagenesis | 276 | No effect on interaction with RET. Binds slightly to SRC, this interaction is independent of SRC phosphorylation. Strongly decreases SRC ubiquitination. Abolishes interaction with EGFR. | ||||
Sequence: G → E | ||||||
Mutagenesis | 341 | Induces E3 activity and autoubiquitination. Releases ubiquitin-conjugating enzyme E2 UBE2D2 faster. | ||||
Sequence: Y → E | ||||||
Mutagenesis | 341 | Abolishes activation by EGF stimulation and enhancement by TGFB1I1 of E3 activity. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 341 | Abolishes E3 activity. | ||||
Sequence: Missing | ||||||
Mutagenesis | 351 | No effect on TGFB1I1 and SRC interactions. Abolishes SRC ubiquitination. Abolishes interaction with TGFB1I1; when associated with A-366. Abolishes interaction with RET and inhibition of RET degradation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 366 | Abolishes interaction with TGFB1I1. Abolishes interaction with TGFB1I1; when associated with A-351. | ||||
Sequence: C → A | ||||||
Natural variant | VAR_018298 | 405 | in dbSNP:rs3208856 | |||
Sequence: H → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 660 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000055866 | 1-474 | UniProt | E3 ubiquitin-protein ligase CBL-C | |||
Sequence: MALAVAPWGRQWEEARALGRAVRMLQRLEEQCVDPRLSVSPPSLRDLLPRTAQLLREVAHSRRAAGGGGPGGPGGSGDFLLIYLANLEAKSRQVAALLPPRGRRSANDELFRAGSRLRRQLAKLAIIFSHMHAELHALFPGGKYCGHMYQLTKAPAHTFWRESCGARCVLPWAEFESLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLKNWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGKTHNPDLTELGQAEPQQRIHVSEEQLQLYWAMDSTFELCKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGWEAVSIYQFHGQATAEDSGNSSDQEGRELELGQVPLSAPPLPPRPDLPPRKPRNAQPKVRLLKGNSPPAALGPQDPAPA | |||||||
Modified residue | 341 | UniProt | Phosphotyrosine; by SRC | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 461 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9ULV8 | ATXN1 P54253 | 6 | EBI-2341018, EBI-930964 | |
BINARY | Q9ULV8 | TARDBP Q13148 | 3 | EBI-2341018, EBI-372899 | |
BINARY | Q9ULV8 | UBE2K P61086 | 3 | EBI-2341018, EBI-473850 | |
BINARY | Q9ULV8 | YES1 P07947 | 3 | EBI-2341018, EBI-515331 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, zinc finger, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 7-145 | 4H | ||||
Sequence: PWGRQWEEARALGRAVRMLQRLEEQCVDPRLSVSPPSLRDLLPRTAQLLREVAHSRRAAGGGGPGGPGGSGDFLLIYLANLEAKSRQVAALLPPRGRRSANDELFRAGSRLRRQLAKLAIIFSHMHAELHALFPGGKYC | ||||||
Domain | 7-321 | Cbl-PTB | ||||
Sequence: PWGRQWEEARALGRAVRMLQRLEEQCVDPRLSVSPPSLRDLLPRTAQLLREVAHSRRAAGGGGPGGPGGSGDFLLIYLANLEAKSRQVAALLPPRGRRSANDELFRAGSRLRRQLAKLAIIFSHMHAELHALFPGGKYCGHMYQLTKAPAHTFWRESCGARCVLPWAEFESLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLFQPWPTLLKNWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGKTHNPDLTE | ||||||
Region | 146-218 | EF-hand-like | ||||
Sequence: GHMYQLTKAPAHTFWRESCGARCVLPWAEFESLLGTCHPVEPGCTALALRTTIDLTCSGHVSIFEFDVFTRLF | ||||||
Region | 219-321 | SH2-like | ||||
Sequence: QPWPTLLKNWQLLAVNHPGYMAFLTYDEVQERLQACRDKPGSYIFRPSCTRLGQWAIGYVSSDGSILQTIPANKPLSQVLLEGQKDGFYLYPDGKTHNPDLTE | ||||||
Region | 322-350 | Linker | ||||
Sequence: LGQAEPQQRIHVSEEQLQLYWAMDSTFEL | ||||||
Zinc finger | 351-390 | RING-type | ||||
Sequence: CKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCR | ||||||
Region | 351-474 | Interaction with RET | ||||
Sequence: CKICAESNKDVKIEPCGHLLCSCCLAAWQHSDSQTCPFCRCEIKGWEAVSIYQFHGQATAEDSGNSSDQEGRELELGQVPLSAPPLPPRPDLPPRKPRNAQPKVRLLKGNSPPAALGPQDPAPA | ||||||
Region | 409-474 | Disordered | ||||
Sequence: TAEDSGNSSDQEGRELELGQVPLSAPPLPPRPDLPPRKPRNAQPKVRLLKGNSPPAALGPQDPAPA | ||||||
Compositional bias | 431-447 | Pro residues | ||||
Sequence: LSAPPLPPRPDLPPRKP |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9ULV8-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsLong
- Length474
- Mass (Da)52,456
- Last updated2007-02-06 v3
- Checksum202634AEDE434544
Q9ULV8-2
- Name2
- SynonymsShort
- Differences from canonical
- 261-306: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y647 | A0A2R8Y647_HUMAN | CBLC | 182 |
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 234 | in Ref. 1; BAA86298 | ||||
Sequence: N → T | ||||||
Alternative sequence | VSP_005732 | 261-306 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 413 | in Ref. 3; AAH28915 | ||||
Sequence: S → P | ||||||
Compositional bias | 431-447 | Pro residues | ||||
Sequence: LSAPPLPPRPDLPPRKP |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB028645 EMBL· GenBank· DDBJ | BAA86298.1 EMBL· GenBank· DDBJ | mRNA | ||
AF117646 EMBL· GenBank· DDBJ | AAD34341.1 EMBL· GenBank· DDBJ | mRNA | ||
AF117647 EMBL· GenBank· DDBJ | AAD34342.1 EMBL· GenBank· DDBJ | mRNA | ||
BC028915 EMBL· GenBank· DDBJ | AAH28915.1 EMBL· GenBank· DDBJ | mRNA |